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P99024

- TBB5_MOUSE

UniProt

P99024 - TBB5_MOUSE

Protein

Tubulin beta-5 chain

Gene

Tubb5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi140 – 1467GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: MGI

    GO - Biological processi

    1. microtubule-based process Source: UniProtKB
    2. protein folding Source: Reactome
    3. protein polymerization Source: InterPro
    4. spindle assembly Source: MGI

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta-5 chain
    Gene namesi
    Name:Tubb5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:107812. Tubb5.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: Ensembl
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: Ensembl
    4. microtubule Source: MGI
    5. nuclear envelope lumen Source: Ensembl
    6. nucleus Source: MGI
    7. plasma membrane Source: Ensembl
    8. tubulin complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Tubulin beta-5 chainPRO_0000048246Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
    Modified residuei58 – 581N6-succinyllysine; alternate1 Publication
    Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
    Modified residuei318 – 3181Omega-N-methylarginineBy similarity
    Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP99024.
    PRIDEiP99024.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00117352.
    P99024.
    SWISS-2DPAGEP99024.

    PTM databases

    PhosphoSiteiP99024.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

    Gene expression databases

    ArrayExpressiP99024.
    BgeeiP99024.
    CleanExiMM_TUBB5.
    GenevestigatoriP99024.

    Interactioni

    Subunit structurei

    Interacts with MX1 By similarity. Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO. May interact with RNABP10.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi204381. 30 interactions.
    IntActiP99024. 32 interactions.
    MINTiMINT-1869561.

    Structurei

    3D structure databases

    ProteinModelPortaliP99024.
    SMRiP99024. Positions 2-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00750000117394.
    HOVERGENiHBG000089.
    InParanoidiB1B178.
    KOiK07375.
    OMAiTPPPHIF.
    OrthoDBiEOG71ZP1H.
    PhylomeDBiP99024.
    TreeFamiTF300298.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR013838. Beta-tubulin_BS.
    IPR002453. Beta_tubulin.
    IPR008280. Tub_FtsZ_C.
    IPR000217. Tubulin.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR023123. Tubulin_C.
    IPR017975. Tubulin_CS.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view]
    PANTHERiPTHR11588. PTHR11588. 1 hit.
    PfamiPF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view]
    PRINTSiPR01163. BETATUBULIN.
    PR01161. TUBULIN.
    SMARTiSM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    PROSITEiPS00227. TUBULIN. 1 hit.
    PS00228. TUBULIN_B_AUTOREG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P99024-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY    50
    YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 300
    AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA 444
    Length:444
    Mass (Da):49,671
    Last modified:August 13, 1987 - v1
    Checksum:i1E6CD0A36773A103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Q → P in BAB27292. (PubMed:16141072)Curated
    Sequence conflicti114 – 1141D → N in BAE40217. (PubMed:16141072)Curated
    Sequence conflicti143 – 1431T → N in BAE28709. (PubMed:16141072)Curated
    Sequence conflicti264 – 2641H → D in BAE40217. (PubMed:16141072)Curated
    Sequence conflicti307 – 3071H → N in BAE39835. (PubMed:16141072)Curated
    Sequence conflicti357 – 3571P → T in BAE40217. (PubMed:16141072)Curated
    Sequence conflicti400 – 4001G → A in AAA40510. (PubMed:3839797)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04663 mRNA. Translation: CAA28369.1.
    AK010960 mRNA. Translation: BAB27292.1.
    AK011263 mRNA. Translation: BAB27504.1.
    AK051164 mRNA. Translation: BAC34541.1.
    AK051393 mRNA. Translation: BAC34623.1.
    AK083327 mRNA. Translation: BAC38866.1.
    AK146567 mRNA. Translation: BAE27265.1.
    AK148978 mRNA. Translation: BAE28709.1.
    AK151215 mRNA. Translation: BAE30210.1.
    AK151670 mRNA. Translation: BAE30596.1.
    AK160225 mRNA. Translation: BAE35700.1.
    AK161575 mRNA. Translation: BAE36471.1.
    AK165249 mRNA. Translation: BAE38103.1.
    AK167691 mRNA. Translation: BAE39738.1.
    AK167779 mRNA. Translation: BAE39811.1.
    AK167808 mRNA. Translation: BAE39835.1.
    AK167926 mRNA. Translation: BAE39931.1.
    AK168271 mRNA. Translation: BAE40217.1.
    AK169123 mRNA. Translation: BAE40903.1.
    AK169210 mRNA. Translation: BAE40982.1.
    AK169295 mRNA. Translation: BAE41051.1.
    CR974451 Genomic DNA. Translation: CAO77890.1.
    BC003825 mRNA. Translation: AAH03825.1.
    M28732 mRNA. Translation: AAA40510.1.
    CCDSiCCDS28706.1.
    PIRiE25437.
    RefSeqiNP_035785.1. NM_011655.5.
    UniGeneiMm.273538.
    Mm.472638.

    Genome annotation databases

    EnsembliENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
    GeneIDi22154.
    KEGGimmu:22154.
    UCSCiuc008ciq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04663 mRNA. Translation: CAA28369.1 .
    AK010960 mRNA. Translation: BAB27292.1 .
    AK011263 mRNA. Translation: BAB27504.1 .
    AK051164 mRNA. Translation: BAC34541.1 .
    AK051393 mRNA. Translation: BAC34623.1 .
    AK083327 mRNA. Translation: BAC38866.1 .
    AK146567 mRNA. Translation: BAE27265.1 .
    AK148978 mRNA. Translation: BAE28709.1 .
    AK151215 mRNA. Translation: BAE30210.1 .
    AK151670 mRNA. Translation: BAE30596.1 .
    AK160225 mRNA. Translation: BAE35700.1 .
    AK161575 mRNA. Translation: BAE36471.1 .
    AK165249 mRNA. Translation: BAE38103.1 .
    AK167691 mRNA. Translation: BAE39738.1 .
    AK167779 mRNA. Translation: BAE39811.1 .
    AK167808 mRNA. Translation: BAE39835.1 .
    AK167926 mRNA. Translation: BAE39931.1 .
    AK168271 mRNA. Translation: BAE40217.1 .
    AK169123 mRNA. Translation: BAE40903.1 .
    AK169210 mRNA. Translation: BAE40982.1 .
    AK169295 mRNA. Translation: BAE41051.1 .
    CR974451 Genomic DNA. Translation: CAO77890.1 .
    BC003825 mRNA. Translation: AAH03825.1 .
    M28732 mRNA. Translation: AAA40510.1 .
    CCDSi CCDS28706.1.
    PIRi E25437.
    RefSeqi NP_035785.1. NM_011655.5.
    UniGenei Mm.273538.
    Mm.472638.

    3D structure databases

    ProteinModelPortali P99024.
    SMRi P99024. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204381. 30 interactions.
    IntActi P99024. 32 interactions.
    MINTi MINT-1869561.

    Chemistry

    BindingDBi P99024.

    PTM databases

    PhosphoSitei P99024.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00117352.
    P99024.
    SWISS-2DPAGE P99024.

    Proteomic databases

    MaxQBi P99024.
    PRIDEi P99024.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001566 ; ENSMUSP00000001566 ; ENSMUSG00000001525 .
    GeneIDi 22154.
    KEGGi mmu:22154.
    UCSCi uc008ciq.2. mouse.

    Organism-specific databases

    CTDi 22154.
    MGIi MGI:107812. Tubb5.

    Phylogenomic databases

    GeneTreei ENSGT00750000117394.
    HOVERGENi HBG000089.
    InParanoidi B1B178.
    KOi K07375.
    OMAi TPPPHIF.
    OrthoDBi EOG71ZP1H.
    PhylomeDBi P99024.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi TUBB. mouse.
    NextBioi 302074.
    PROi P99024.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P99024.
    Bgeei P99024.
    CleanExi MM_TUBB5.
    Genevestigatori P99024.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR013838. Beta-tubulin_BS.
    IPR002453. Beta_tubulin.
    IPR008280. Tub_FtsZ_C.
    IPR000217. Tubulin.
    IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
    IPR023123. Tubulin_C.
    IPR017975. Tubulin_CS.
    IPR003008. Tubulin_FtsZ_GTPase.
    [Graphical view ]
    PANTHERi PTHR11588. PTHR11588. 1 hit.
    Pfami PF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01163. BETATUBULIN.
    PR01161. TUBULIN.
    SMARTi SM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    PROSITEi PS00227. TUBULIN. 1 hit.
    PS00228. TUBULIN_B_AUTOREG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype."
      Wang D., Villasante A., Lewis S.A., Cowan N.J.
      J. Cell Biol. 103:1903-1910(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta, Spinal ganglion, Spleen, Sympathetic ganglion and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297; 310-318; 321-359 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "Five mouse tubulin isotypes and their regulated expression during development."
      Lewis S.A., Lee M.G.-S., Cowan N.J.
      J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
    7. Cited for: POLYGLUTAMYLATION.
    8. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
      Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
      J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP10.
    9. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
      Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
      Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYGLYCYLATION.
    10. Cited for: INTERACTION WITH PIFO.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTBB5_MOUSE
    AccessioniPrimary (citable) accession number: P99024
    Secondary accession number(s): B1B178
    , P05218, Q3TFB6, Q3THH9, Q3TIL1, Q3UAV4, Q3UF52, Q8WUC1, Q9CY33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3